Linked Life Data

8662926

Source:http://linkedlifedata.com/resource/pubmed/id/8662926

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
25
pubmed:dateCreated
1996-8-13
pubmed:abstractText
Hexokinase II (HKII) is the predominant isozyme expressed in peripheral insulin-responsive tissues. To explore the role of HKII in muscle glucose metabolism, two lines of transgenic mice were generated where overexpression was restricted to striated muscle; HKII protein levels and activity were increased by 3-8-fold. Oral glucose tolerance, intravenous insulin tolerance, and insulin and lactate levels were unaffected in transgenic mice. There was a trend toward increased levels of muscle glycogen; however, glucose-6-phosphate levels were increased by 43% in transgenic skeletal muscle following in vivo glucose and insulin administration. Using 2-[3H]deoxyglucose as a tracer, in vitro basal and insulin-stimulated glucose uptake were determined in extensor digitorum longus, soleus, and epitrochlearis muscles. Maximal insulin-stimulated glucose uptake was increased by 17% (extensor digitorum longus), 34% (soleus), and 90% (epitrochlearis) in transgenic muscles; basal and submaximal glucose uptake was also modestly increased in soleus and epitrochlearis. These data suggest that increased muscle HKII (corresponding to the upper end of the physiologic range) may not be sufficient to augment net in vivo glucose homeostasis. However, glucose phosphorylation can represent a rate-limiting step for skeletal muscle glucose utilization since muscle glucose-6-phosphate levels are increased during in vivo hyperinsulinemia and hyperglycemia; furthermore, basal and insulin-mediated muscle glucose uptake can be increased by a selective increase in HKII expression.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
21
pubmed:volume
271
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
14834-9
pubmed:dateRevised
2011-11-17
pubmed:meshHeading
pubmed-meshheading:8662926-Amino Acid Sequence, pubmed-meshheading:8662926-Animals, pubmed-meshheading:8662926-Antibodies, pubmed-meshheading:8662926-Blood Glucose, pubmed-meshheading:8662926-Creatine Kinase, pubmed-meshheading:8662926-Eating, pubmed-meshheading:8662926-Enhancer Elements, Genetic, pubmed-meshheading:8662926-Fasting, pubmed-meshheading:8662926-Female, pubmed-meshheading:8662926-Gene Expression, pubmed-meshheading:8662926-Genetic Vectors, pubmed-meshheading:8662926-Glucose, pubmed-meshheading:8662926-Glucose Tolerance Test, pubmed-meshheading:8662926-Hexokinase, pubmed-meshheading:8662926-Humans, pubmed-meshheading:8662926-Insulin, pubmed-meshheading:8662926-Isoenzymes, pubmed-meshheading:8662926-Lactates, pubmed-meshheading:8662926-Male, pubmed-meshheading:8662926-Mice, pubmed-meshheading:8662926-Mice, Inbred Strains, pubmed-meshheading:8662926-Mice, Transgenic, pubmed-meshheading:8662926-Molecular Sequence Data, pubmed-meshheading:8662926-Muscle, Skeletal, pubmed-meshheading:8662926-Peptides, pubmed-meshheading:8662926-Phosphorylation, pubmed-meshheading:8662926-Promoter Regions, Genetic, pubmed-meshheading:8662926-Rats, pubmed-meshheading:8662926-Restriction Mapping
pubmed:year
1996
pubmed:articleTitle
Overexpression of hexokinase II in transgenic mice. Evidence that increased phosphorylation augments muscle glucose uptake.
pubmed:affiliation
Department of Medicine, Beth Israel Hospital and Harvard Medical School, Boston, Massachusetts 02215, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't